ID C9K0Z0_MOUSE Unreviewed; 883 AA. AC C9K0Z0; DT 24-NOV-2009, integrated into UniProtKB/TrEMBL. DT 24-NOV-2009, sequence version 1. DT 29-SEP-2021, entry version 66. DE RecName: Full=Glutamate receptor {ECO:0000256|RuleBase:RU367118}; GN Name=Gria2 {ECO:0000313|MGI:MGI:95809}; GN Synonyms=glur-2 {ECO:0000313|EMBL:BAI44626.1}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:BAI44626.1}; RN [1] {ECO:0000313|EMBL:BAI44626.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=DdY {ECO:0000313|EMBL:BAI44626.1}; RC TISSUE=Spinal cord {ECO:0000313|EMBL:BAI44626.1}; RA Nishizawa M., Ito S.; RT "Expression of AMPA receptor subtypes in mouse spinal cord."; RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0007829|PDB:7LEP} RP STRUCTURE BY ELECTRON MICROSCOPY (3.25 ANGSTROMS) OF 417-840, AND DISULFIDE RP BONDS. RX PubMed=33981040; DOI=10.1038/s41586-021-03540-0; RA Yu J., Rao P., Clark S., Mitra J., Ha T., Gouaux E.; RT "Hippocampal AMPA receptor assemblies and mechanism of allosteric RT inhibition."; RL Nature 0:0-0(2021). CC -!- FUNCTION: Receptor for glutamate that functions as a ligand-gated ion CC channel in the central nervous system and plays an important role in CC excitatory synaptic transmission. L-glutamate acts as an excitatory CC neurotransmitter at many synapses in the central nervous system. CC {ECO:0000256|RuleBase:RU367118}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU367118}; CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}. Cell CC junction, synapse, postsynaptic cell membrane CC {ECO:0000256|RuleBase:RU367118}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1) CC family. {ECO:0000256|RuleBase:RU367118}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB109210; BAI44626.1; -; mRNA. DR PDB; 7LEP; EM; 3.25 A; B/D=417-840. DR PeptideAtlas; C9K0Z0; -. DR MGI; MGI:95809; Gria2. DR OMA; IRKEADM; -. DR ChiTaRS; Gria2; mouse. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IEA:InterPro. DR InterPro; IPR001828; ANF_lig-bd_rcpt. DR InterPro; IPR019594; Glu/Gly-bd. DR InterPro; IPR001508; Iono_rcpt_met. DR InterPro; IPR001320; Iontro_rcpt. DR InterPro; IPR028082; Peripla_BP_I. DR Pfam; PF01094; ANF_receptor; 1. DR Pfam; PF00060; Lig_chan; 1. DR Pfam; PF10613; Lig_chan-Glu_bd; 1. DR PRINTS; PR00177; NMDARECEPTOR. DR SMART; SM00918; Lig_chan-Glu_bd; 1. DR SMART; SM00079; PBPe; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:7LEP}; KW Cell junction {ECO:0000256|ARBA:ARBA00022949, KW ECO:0000256|RuleBase:RU367118}; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, KW ECO:0000256|RuleBase:RU367118}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Ion channel {ECO:0000256|ARBA:ARBA00023303, ECO:0000256|RuleBase:RU367118}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, KW ECO:0000256|RuleBase:RU367118}; KW Ligand-gated ion channel {ECO:0000256|ARBA:ARBA00023286, KW ECO:0000256|RuleBase:RU367118}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367118}; KW Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00023257, KW ECO:0000256|RuleBase:RU367118}; KW Receptor {ECO:0000256|RuleBase:RU367118, ECO:0000313|EMBL:BAI44626.1}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU367118}; KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU367118}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, KW ECO:0000256|RuleBase:RU367118}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|RuleBase:RU367118}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU367118}. FT SIGNAL 1..24 FT /evidence="ECO:0000256|RuleBase:RU367118" FT CHAIN 25..883 FT /note="Glutamate receptor" FT /evidence="ECO:0000256|RuleBase:RU367118" FT /id="PRO_5027162428" FT TRANSMEM 542..564 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367118" FT TRANSMEM 625..647 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367118" FT TRANSMEM 815..837 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU367118" FT DOMAIN 415..790 FT /note="PBPe" FT /evidence="ECO:0000259|SMART:SM00079" FT DOMAIN 425..490 FT /note="Lig_chan-Glu_bd" FT /evidence="ECO:0000259|SMART:SM00918" FT DISULFID 739..794 FT /evidence="ECO:0007829|PDB:7LEP" SQ SEQUENCE 883 AA; 98574 MW; 9BBE632C31CB01FF CRC64; MQKIMHISVL LSPVLWGLIF GVSSNSIQIG GLFPRGADQE YSAFRVGMVQ FSTSEFRLTP HIDNLEVANS FAVTNAFCSQ FSRGVYAIFG FYDKKSVNTI TSFCGTLHVS FITPSFPTDG THPFVIQMRP DLKGALLSLI EYYQWDKFAY LYDSDRGLST LQAVLDSAAE KKWQVTAINV GNINNDKKDE TYRSLFQDLE LKKERRVILD CERDKVNDIV DQVITIGKHV KGYHYIIANL GFTDGDLLKI QFGGANVSGF QIVVYDDSLA SKFIERWSTL EGKEYPGAHT ATIKYTSALT YDAVQVMTEA FRNLRKQRIE ISRRGNAGDC LANPAVPWGQ GVEIERALKQ VQVEGLSGNI KFDQNGKRIN YTINIMELKT NGPRKIGYWS EVDKMVVTLT ELPSGNDTSG LENKTVVVTT ILESPYVMMK KNHEMLEGNE RYEGYCVDLA AEIAKHCGFK YKLTIVGDGK YGARDADTKI WNGMVGELVY GKADIAIAPL TITLVREEVI DFSKPFMSLG ISIMIKKPQK SKPGVFSFLD PLAYEIWMCI VFAYIGVSVV LFLVSRFSPY EWHTEEFEDG RETQSSESTN EFGIFNSLWF SLGAFMRQGC DISPRSLSGR IVGGVWWFFT LIIISSYTAN LAAFLTVERM VSPIESAEDL SKQTEIAYGT LDSGSTKEFF RRSKIAVFDK MWTYMRSAEP SVFVRTTAEG VARVRKSKGK YAYLLESTMN EYIEQRKPCD TMKVGGNLDS KGYGIATPKG SSLGNAVNLA VLKLNEQGLL DKLKNKWWYD KGECGSGGGD SKEKTSALSL SNVAGVFYIL VGGLGLAMLV ALIEFCYKSR AEAKRMKVAK NAQNINPSSS QNSQNFATYK EGYNVYGIES VKI //